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3EKG

CRYSTAL STRUCTURE OF L-RHAMNONATE DEHYDRATASE FROM AZOTOBACTER VINELANDII complexed with Mg and L-TARTRATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0046872molecular_functionmetal ion binding
A0050032molecular_functionL-rhamnonate dehydratase activity
B0000287molecular_functionmagnesium ion binding
B0009063biological_processamino acid catabolic process
B0016052biological_processcarbohydrate catabolic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0046872molecular_functionmetal ion binding
B0050032molecular_functionL-rhamnonate dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TLA A 501
ChainResidue
AHIS24
ALEU342
AMG601
AHOH617
AARG50
ALYS179
AASP216
ATRP218
AGLU242
AGLU270
AHIS320
AGLU340

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AASP216
AGLU242
AGLU270
ATLA501
AHOH617

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TLA B 502
ChainResidue
BHIS24
BARG50
BLYS179
BASP216
BTRP218
BGLU242
BGLU270
BHIS320
BGLU340
BLEU342
BMG602
BHOH825
BHOH992

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 602
ChainResidue
BASP216
BGLU242
BGLU270
BTLA502
BHOH825

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. TiSGVDlALwDLlGKvrrePVhqLLG
ChainResidueDetails
ATHR126-GLY151

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PDB entries from 2026-01-28

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